ID SMC2_HUMAN Reviewed; 1197 AA. AC O95347; Q6IEE0; Q9P1P2; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 11-NOV-2015, entry version 137. DE RecName: Full=Structural maintenance of chromosomes protein 2; DE Short=SMC protein 2; DE Short=SMC-2; DE AltName: Full=Chromosome-associated protein E; DE Short=hCAP-E; DE AltName: Full=XCAP-E homolog; GN Name=SMC2; Synonyms=CAPE, SMC2L1; ORFNames=PRO0324; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SMC4. RC TISSUE=Teratocarcinoma; RX PubMed=9789013; DOI=10.1073/pnas.95.22.12906; RA Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S., RA Yokomori K.; RT "Identification of two distinct human SMC protein complexes involved RT in mitotic chromosome dynamics."; RL Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., RA Zhou W., Bi J., Zhang Y., Liu M., He F.; RT "Functional prediction of the coding sequences of 32 new genes deduced RT by analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP IDENTIFICATION. RX PubMed=14660695; DOI=10.1093/molbev/msh023; RA Cobbe N., Heck M.M.S.; RT "The evolution of SMC proteins: phylogenetic analysis and structural RT implications."; RL Mol. Biol. Evol. 21:332-347(2004). RN [8] RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 AND CNAP1, AND RP SUBCELLULAR LOCATION. RX PubMed=10958694; DOI=10.1128/MCB.20.18.6996-7006.2000; RA Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.; RT "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a RT homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 RT during the early stage of mitotic chromosome condensation."; RL Mol. Cell. Biol. 20:6996-7006(2000). RN [9] RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRRN1; CNAP1 AND RP CAPG, AND FUNCTION OF THE COMPLEX. RX PubMed=11136719; DOI=10.1074/jbc.C000873200; RA Kimura K., Cuvier O., Hirano T.; RT "Chromosome condensation by a human condensin complex in Xenopus egg RT extracts."; RL J. Biol. Chem. 276:5417-5420(2001). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677; RP LYS-1158 AND LYS-1160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP INTERACTION WITH BRD4. RX PubMed=23728299; DOI=10.1038/nature12147; RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., RA Cannell I.G., Bryson B.D., Rameseder J., Lee M.J., Blake E.J., RA Fydrych A., Ho R., Greenberger B.A., Chen G.C., Maffa A., RA Del Rosario A.M., Root D.E., Carpenter A.E., Hahn W.C., Sabatini D.M., RA Chen C.C., White F.M., Bradner J.E., Yaffe M.B.; RT "The bromodomain protein Brd4 insulates chromatin from DNA damage RT signalling."; RL Nature 498:246-250(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Central component of the condensin complex, a complex CC required for conversion of interphase chromatin into mitotic-like CC condense chromosomes. The condensin complex probably introduces CC positive supercoils into relaxed DNA in the presence of type I CC topoisomerases and converts nicked DNA into positive knotted forms CC in the presence of type II topoisomerases. CC {ECO:0000269|PubMed:11136719}. CC -!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin CC complex, which contains the SMC2 and SMC4 heterodimer, and three CC non SMC subunits that probably regulate the complex: BRRN1/CAPH, CC CNAP1/CAPD2 and CAPG. Interacts with BRD4 (isoform B), leading to CC insulate chromatin from DNA damage response pathway. CC {ECO:0000269|PubMed:10958694, ECO:0000269|PubMed:11136719, CC ECO:0000269|PubMed:23728299, ECO:0000269|PubMed:9789013}. CC -!- INTERACTION: CC Q15003:NCAPH; NbExp=2; IntAct=EBI-355822, EBI-1046410; CC Q6IBW4:NCAPH2; NbExp=2; IntAct=EBI-355822, EBI-2548296; CC Q9NTJ3:SMC4; NbExp=3; IntAct=EBI-355822, EBI-356173; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. CC Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome CC {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the CC majority of the condensin complex is found in the cytoplasm, while CC a minority of the complex is associated with chromatin. A CC subpopulation of the complex however remains associated with CC chromosome foci in interphase cells. During mitosis, most of the CC condensin complex is associated with the chromatin. At the onset CC of prophase, the regulatory subunits of the complex are CC phosphorylated by CDC2, leading to condensin's association with CC chromosome arms and to chromosome condensation. Dissociation from CC chromosomes is observed in late telophase. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95347-1; Sequence=Displayed; CC Name=2; CC IsoId=O95347-2; Sequence=VSP_007243, VSP_007244; CC Note=No experimental confirmation available.; CC -!- DOMAIN: The hinge domain, which separates the large intramolecular CC coiled coil regions, allows the heterodimerization with SMC4, CC forming a V-shaped heterodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72360.1; Type=Frameshift; Positions=890, 908; Evidence={ECO:0000305}; CC Sequence=AAF29579.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF092563; AAC72360.1; ALT_FRAME; mRNA. DR EMBL; AL833191; CAI46187.1; -; mRNA. DR EMBL; AL161791; CAI16866.1; -; Genomic_DNA. DR EMBL; AL354938; CAI16866.1; JOINED; Genomic_DNA. DR EMBL; AL354938; CAI16923.1; -; Genomic_DNA. DR EMBL; AL161791; CAI16923.1; JOINED; Genomic_DNA. DR EMBL; CH471105; EAW58973.1; -; Genomic_DNA. DR EMBL; BC130385; AAI30386.1; -; mRNA. DR EMBL; AF113673; AAF29579.1; ALT_INIT; mRNA. DR EMBL; BN000163; CAD89875.1; -; mRNA. DR CCDS; CCDS35086.1; -. [O95347-1] DR RefSeq; NP_001036015.1; NM_001042550.1. [O95347-1] DR RefSeq; NP_001036016.1; NM_001042551.1. [O95347-1] DR RefSeq; NP_001252531.1; NM_001265602.1. [O95347-1] DR RefSeq; NP_006435.2; NM_006444.2. [O95347-1] DR RefSeq; XP_006716996.1; XM_006716933.2. [O95347-1] DR RefSeq; XP_011516450.1; XM_011518148.1. [O95347-1] DR RefSeq; XP_011516451.1; XM_011518149.1. [O95347-1] DR RefSeq; XP_011516455.1; XM_011518153.1. [O95347-2] DR UniGene; Hs.119023; -. DR PDB; 4U4P; X-ray; 1.89 A; A=476-707. DR PDBsum; 4U4P; -. DR ProteinModelPortal; O95347; -. DR SMR; O95347; 506-660. DR BioGrid; 115841; 48. DR DIP; DIP-35422N; -. DR IntAct; O95347; 15. DR MINT; MINT-1161754; -. DR STRING; 9606.ENSP00000286398; -. DR PhosphoSite; O95347; -. DR BioMuta; SMC2; -. DR MaxQB; O95347; -. DR PaxDb; O95347; -. DR PRIDE; O95347; -. DR Ensembl; ENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1] DR Ensembl; ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1] DR Ensembl; ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1] DR GeneID; 10592; -. DR KEGG; hsa:10592; -. DR UCSC; uc004bbv.3; human. [O95347-1] DR CTD; 10592; -. DR GeneCards; SMC2; -. DR H-InvDB; HIX0008250; -. DR HGNC; HGNC:14011; SMC2. DR MIM; 605576; gene. DR neXtProt; NX_O95347; -. DR PharmGKB; PA37833; -. DR eggNOG; KOG0933; Eukaryota. DR eggNOG; COG1196; LUCA. DR GeneTree; ENSGT00550000074857; -. DR HOGENOM; HOG000228249; -. DR HOVERGEN; HBG106605; -. DR InParanoid; O95347; -. DR KO; K06674; -. DR OMA; CQNGKIP; -. DR OrthoDB; EOG7SR4KV; -. DR PhylomeDB; O95347; -. DR TreeFam; TF101157; -. DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes. DR ChiTaRS; SMC2; human. DR GeneWiki; SMC2; -. DR GenomeRNAi; 10592; -. DR NextBio; 40225; -. DR PRO; PR:O95347; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; O95347; -. DR CleanEx; HS_SMC2; -. DR ExpressionAtlas; O95347; baseline and differential. DR Genevisible; O95347; HS. DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB. DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051383; P:kinetochore organization; IEA:Ensembl. DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:Ensembl. DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:Ensembl. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR027120; Smc2. DR InterPro; IPR010935; SMC_hinge. DR PANTHER; PTHR18937:SF9; PTHR18937:SF9; 1. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 2. DR PIRSF; PIRSF005719; SMC; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; KW Cytoplasm; DNA condensation; Mitosis; Nucleotide-binding; Nucleus; KW Polymorphism; Reference proteome. FT CHAIN 1 1197 Structural maintenance of chromosomes FT protein 2. FT /FTId=PRO_0000118995. FT NP_BIND 32 39 ATP. {ECO:0000255}. FT REGION 508 671 Flexible hinge. FT COILED 173 507 {ECO:0000255}. FT COILED 672 926 {ECO:0000255}. FT COILED 963 1031 {ECO:0000255}. FT COMPBIAS 1085 1120 Ala/Asp-rich (DA-box). FT MOD_RES 114 114 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 222 222 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 677 677 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 1158 1158 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 1160 1160 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT VAR_SEQ 1091 1099 SLVALSLIL -> QKQQNHTTG (in isoform 2). FT {ECO:0000303|Ref.6}. FT /FTId=VSP_007243. FT VAR_SEQ 1100 1197 Missing (in isoform 2). FT {ECO:0000303|Ref.6}. FT /FTId=VSP_007244. FT VARIANT 1009 1009 E -> K (in dbSNP:rs4562395). FT /FTId=VAR_047489. FT CONFLICT 294 294 G -> V (in Ref. 1; AAC72360). FT {ECO:0000305}. FT CONFLICT 916 916 N -> H (in Ref. 1; AAC72360). FT {ECO:0000305}. FT CONFLICT 998 998 Y -> C (in Ref. 1; AAC72360). FT {ECO:0000305}. FT HELIX 476 502 {ECO:0000244|PDB:4U4P}. FT HELIX 504 506 {ECO:0000244|PDB:4U4P}. FT HELIX 519 521 {ECO:0000244|PDB:4U4P}. FT STRAND 522 525 {ECO:0000244|PDB:4U4P}. FT HELIX 526 529 {ECO:0000244|PDB:4U4P}. FT STRAND 531 533 {ECO:0000244|PDB:4U4P}. FT HELIX 535 537 {ECO:0000244|PDB:4U4P}. FT HELIX 538 545 {ECO:0000244|PDB:4U4P}. FT HELIX 546 550 {ECO:0000244|PDB:4U4P}. FT STRAND 552 555 {ECO:0000244|PDB:4U4P}. FT HELIX 557 566 {ECO:0000244|PDB:4U4P}. FT STRAND 573 577 {ECO:0000244|PDB:4U4P}. FT TURN 578 580 {ECO:0000244|PDB:4U4P}. FT HELIX 588 598 {ECO:0000244|PDB:4U4P}. FT STRAND 602 605 {ECO:0000244|PDB:4U4P}. FT HELIX 606 609 {ECO:0000244|PDB:4U4P}. FT HELIX 614 616 {ECO:0000244|PDB:4U4P}. FT HELIX 617 624 {ECO:0000244|PDB:4U4P}. FT STRAND 628 632 {ECO:0000244|PDB:4U4P}. FT HELIX 633 640 {ECO:0000244|PDB:4U4P}. FT TURN 643 645 {ECO:0000244|PDB:4U4P}. FT STRAND 649 651 {ECO:0000244|PDB:4U4P}. FT STRAND 656 658 {ECO:0000244|PDB:4U4P}. FT TURN 659 661 {ECO:0000244|PDB:4U4P}. FT STRAND 662 666 {ECO:0000244|PDB:4U4P}. FT HELIX 674 704 {ECO:0000244|PDB:4U4P}. SQ SEQUENCE 1197 AA; 135656 MW; 15EBB56B31FC1364 CRC64; MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV //